+Open data
-Basic information
Entry | Database: PDB / ID: 1mvf | ||||||
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Title | MazE addiction antidote | ||||||
Components |
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Keywords | IMMUNE SYSTEM / plasmid addiction / camel antibody / addiction antidote | ||||||
Function / homology | Function and homology information toxin sequestering activity / toxin-antitoxin complex / single-species biofilm formation / regulation of growth / double-stranded DNA binding / regulation of DNA-templated transcription / protein-containing complex binding / protein homodimerization activity / protein-containing complex / DNA binding Similarity search - Function | ||||||
Biological species | Camelus dromedarius (Arabian camel) Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.65 Å | ||||||
Authors | Loris, R. / Marianovsky, I. / Lah, J. / Laeremans, T. / Engelberg-Kulka, H. / Glaser, G. / Muyldermans, S. / Wyns, L. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2003 Title: Crystal structure of the intrinsically flexible addiction antidote MazE. Authors: Loris, R. / Marianovsky, I. / Lah, J. / Laeremans, T. / Engelberg-Kulka, H. / Glaser, G. / Muyldermans, S. / Wyns, L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mvf.cif.gz | 75.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mvf.ent.gz | 59.8 KB | Display | PDB format |
PDBx/mmJSON format | 1mvf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1mvf_validation.pdf.gz | 453.9 KB | Display | wwPDB validaton report |
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Full document | 1mvf_full_validation.pdf.gz | 460.2 KB | Display | |
Data in XML | 1mvf_validation.xml.gz | 16.7 KB | Display | |
Data in CIF | 1mvf_validation.cif.gz | 23.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mv/1mvf ftp://data.pdbj.org/pub/pdb/validation_reports/mv/1mvf | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Details | MazE-cabmaz1 complex. MazE is a dimer. Each MazE monomer has one monomer of cabmaz1 bound |
-Components
#1: Antibody | Mass: 14891.463 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Camelus dromedarius (Arabian camel) / Production host: Escherichia coli (E. coli) #2: Protein | Mass: 9366.703 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: MazE / Production host: Escherichia coli (E. coli) / References: UniProt: P18534, UniProt: P0AE72*PLUS #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 1.86 Å3/Da / Density % sol: 33.97 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: PEG 8000, magnesium acetate, cacodylic acid, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation |
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Radiation wavelength |
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Reflection | Resolution: 1.65→15 Å / Num. obs: 32058 / % possible obs: 74.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 2.97 % / Rmerge(I) obs: 0.07 / Rsym value: 0.07 / Net I/σ(I): 11.82 | ||||||||||||||||||
Reflection shell | Resolution: 1.65→1.75 Å / % possible all: 57.9 | ||||||||||||||||||
Reflection | *PLUS Num. obs: 32375 / Num. measured all: 96388 / Rmerge(I) obs: 0.07 | ||||||||||||||||||
Reflection shell | *PLUS Lowest resolution: 1.71 Å / % possible obs: 61 % / Num. unique obs: 2633 / Num. measured obs: 4348 / Rmerge(I) obs: 0.228 / Mean I/σ(I) obs: 3.76 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.65→15 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.65→15 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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